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A substrate-optimized electrophoretic mobility shift assay for ADAM12
Alexander Kotzsch, Tine Skovgaard, Uwe Buus, Simon Andersen, Kanchan Devkota, Jens Berthelsen
Protein Production and Characterization Platform
Novo Nordisk Foundation Center for Protein Research
Protein Structure and Function Program
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Dive into the research topics of 'A substrate-optimized electrophoretic mobility shift assay for ADAM12'. Together they form a unique fingerprint.
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Keyphrases
Electrophoretic Mobility Shift Assay
100%
ADAM12
100%
Disintegrin
66%
Metalloprotease
66%
Tumor Necrosis Factor-α
33%
Screening Effort
33%
Drug Target
33%
Excellent Performance
33%
ADAM17
33%
Pharmaceutical Drugs
33%
Epidermal Growth Factor Receptor Ligands
33%
Clinical Testing
33%
Molecular Probe
33%
Tumor Necrosis Factor-α Converting Enzyme
33%
Growth Factors
33%
Biochemical Assay
33%
Peptide Substrate
33%
Large-scale Screening
33%
Protease
33%
Selective Inhibitor
33%
Small Molecule Inhibitors
33%
Biochemistry, Genetics and Molecular Biology
Electrophoretic Mobility Shift Assay
100%
ADAM12
100%
Metalloproteinase
66%
Disintegrin
66%
Tumor Necrosis Factor Alpha
66%
Metalloendopeptidase
66%
Tumor Necrosis Factor
66%
Growth Factor
33%
ADAM17
33%
Enzyme
33%
Protease
33%
Molecular Probe
33%
Epidermal Growth Factor Receptor
33%
Small Molecule
33%
Pharmacology, Toxicology and Pharmaceutical Science
Metalloproteinase
100%
Tumor Necrosis Factor Alpha Converting Enzyme
100%
Disintegrin
100%
Electrophoretic Mobility Shift Assay
100%
Tumor Necrosis Factor
50%
Proteinase
50%
Side Effect
50%
Epidermal Growth Factor Receptor
50%
Growth Factor
50%